EU H2020 Project "TOXICLIPASYN (Understanding the balance between functional and deleterious interactions of..)": description, partecipants, costs and EC-fundings

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toxiclipasyn project word cloud

Explore the words cloud of the toxiclipasyn project. It provides you a very rough idea of what is the project "toxiclipasyn" about.

structures bound disordered modifications native structural responsible stages misfold vitro modulate vesicles spectroscopy plasticity pathology intrinsically nuclear brain synuclein kinetics mice functional ageing lipid equilibrium biological pd hallmark fibril molecules circumstances vivo conformation innovative alpha thorough combination deleterious small proteins amyloid magnetic dichroism parkinson techniques isolated knock helical diseases solution microscopy model neurodegenerative lipids conformations toxic diabetes force switch effect circular thermodynamic resonance gene interplay synthetic membranes function fluorescence atomic disease kinetic composition interaction fulfil physiological protein interactions membrane synaptic form life nature dimensional aggregation bilayers electron propensity structure shown biophysical

Project "toxiclipasyn" data sheet

The following table provides information about the project.

Coordinator	DEUTSCHES ZENTRUM FUR NEURODEGENERATIVE ERKRANKUNGEN EV Organization address address: SIGMUND FREUD STRASSE 27 city: BONN postcode: 53127 website: www.dzne.de contact info title: n.a. name: n.a. surname: n.a. function: n.a. email: n.a. telephone: n.a. fax: n.a.
Coordinator Country	Germany [DE]
Project website	https://www.dzne.de/en/research/research-areas/fundamental-research/research-groups/di-monte/research-areasfocus/
Total cost	171˙460 €
EC max contribution	171˙460 € (100%)
Programme	1. H2020-EU.1.3.2. (Nurturing excellence by means of cross-border and cross-sector mobility)
Code Call	H2020-MSCA-IF-2015
Funding Scheme	MSCA-IF-EF-ST
Starting year	2017
Duration (year-month-day)	from 2017-05-01 to 2019-04-30

#	participants	country	role	EC contrib. [€]
1	DEUTSCHES ZENTRUM FUR NEURODEGENERATIVE ERKRANKUNGEN EV	DE (BONN)	coordinator	171˙460.00

DEUTSCHES ZENTRUM FUR NEURODEGENERATIVE ERKRANKUNGEN EV

DE (BONN)

coordinator

171˙460.00

Project objective

Proteins are among the most essential molecules of life. In order to fulfil their native function(s) they need to adopt a well-defined three-dimensional structure. However, under some circumstances, proteins can misfold and/or form toxic amyloid structures, which are the hallmark of a range of diseases including type 2 diabetes and neurodegenerative diseases. In particular, the small pre-synaptic protein, alpha-synuclein (AS), whose aggregation is the hallmark of Parkinson’s disease, can adopt in vivo and in vitro an intrinsically disordered conformation in solution and an alpha helical state when bound to membranes; the equilibrium between these two conformations has been shown to be important for its proposed native function, e.g. synaptic plasticity, and to modulate its kinetics of fibril formation. Here, I propose to investigate the physiological factors responsible for the switch between functional and deleterious interactions between membrane bilayers and AS due to ageing or disease using an innovative combination of biological, structural, thermodynamic and kinetic studies. In particular, I propose to use both synthetic lipid model systems and isolated synaptic vesicles to study the effect of ageing and the presence of lipids associated with Parkinson’s disease pathology on the nature of the interaction between AS and lipid bilayers. The synaptic vesicles will be isolated from the brain of mice at different ageing stages, as well as from mice carrying gene modifications or knock out related to PD. The interaction between AS and the vesicles will be studied using a range of biophysical techniques including circular dichroism, fluorescence and nuclear magnetic resonance spectroscopy, Atomic Force and Electron Microscopy. The aim of this study is to establish a thorough understanding of the interplay between changes in lipid composition and increased propensity of protein aggregation.

Publications

List of publications.
year	authors and title	journal	last update
2018	James W. P. Brown, Georg Meisl, Tuomas P. J. Knowles, Alexander K. Buell, Christopher M. Dobson, CÃ©line Galvagnion Kinetic barriers to Î±-synuclein protofilament formation and conversion into mature fibrils published pages: 7854-7857, ISSN: 1359-7345, DOI: 10.1039/c8cc03002b	Chemical Communications 54/56	2019-09-25
2018	Ingrid M. van der Wateren, Tuomas P. J. Knowles, Alexander K. Buell, Christopher M. Dobson, CÃ©line Galvagnion C-terminal truncation of Î±-synuclein promotes amyloid fibril amplification at physiological pH published pages: 5506-5516, ISSN: 2041-6520, DOI: 10.1039/c8sc01109e	Chemical Science 9/25	2019-09-25
2018	Michele Perni, Patrick Flagmeier, Ryan Limbocker, Roberta Cascella, Francesco A. Aprile, CÃ©line Galvagnion, Gabriella T. Heller, Georg Meisl, Serene W. Chen, Janet R. Kumita, Pavan K. Challa, Julius B. Kirkegaard, Samuel I. A. Cohen, Benedetta Mannini, Denise Barbut, Ellen A. A. Nollen, Cristina Cecchi, Nunilo Cremades, Tuomas P. J. Knowles, Fabrizio Chiti, Michael Zasloff, Michele Vendruscolo, Christopher M. Dobson Multistep Inhibition of Î±-Synuclein Aggregation and Toxicity in Vitro and in Vivo by Trodusquemine published pages: 2308-2319, ISSN: 1554-8929, DOI: 10.1021/acschembio.8b00466	ACS Chemical Biology 13/8	2019-09-25
2018	Johnny Habchi, Sean Chia, CÃ©line Galvagnion, Thomas C. T. Michaels, Mathias M. J. Bellaiche, Francesco Simone Ruggeri, Michele Sanguanini, Ilaria Idini, Janet R. Kumita, Emma Sparr, Sara Linse, Christopher M. Dobson, Tuomas P. J. Knowles, Michele Vendruscolo Cholesterol catalyses AÎ²42 aggregation through a heterogeneous nucleation pathway in the presence of lipid membranes published pages: 673-683, ISSN: 1755-4330, DOI: 10.1038/s41557-018-0031-x	Nature Chemistry 10/6	2019-09-25

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